ACLS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fujihara, N.
Right arrow Articles by Katsuyama, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fujihara, N.
Right arrow Articles by Katsuyama, T.
Annals of Clinical & Laboratory Science 34:218-225 (2004)
© 2004 Association of Clinical Scientists

Characterization of Factor XII Tenri, a Rare CRM-Negative Factor XII Deficiency

Noriko Fujihara1, Minoru Tozuka1, Kazuyoshi Yamauchi1, Ichiro Ueno1, Nobuyuki Urasawa2, Shinsuke Ishikawa1, Masako Hirota-Kawadobora1, Nobuo Okumura3, Hiroya Hidaka3 and Tsutomu Katsuyama1
1 Department of Laboratory Medicine, Shinshu University Hospital, 2 Third Department of Internal Medicine, Shinshu University School of Medicine, and 3 Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University, Matsumoto, Japan

Address correspondence to Minoru Tozuka, PhD, Department of Laboratory Medicine, Shinshu University Hospital, 3-1-1 Asahi, Matsumoto 390-8621, Japan; tel 81 263 37 2805 fax: 81 263 34 5316; e-mail mtozuka{at}hsp.md.shinshu-u.ac.jp.

Factor XII Tenri (Y34C), a rare cross-reacting material (CRM)-negative factor XII deficiency, was identified in a 71-yr-old Japanese woman with angina pectoris. In the patient’s plasma, factor XII activity and antigen levels were only 1.6% and 5.0%, respectively, of those seen in a normal subject. Immunoblot analysis showed that the secreted factor XII Tenri existed not only as a monomer (76 kDa), but also in complexes with apparent molecular weights of approximately 115, 140, 190, 215, and 225 kDa. After reduction with 2-mercaptoethanol, the factor XII Tenri contained in the complexes was completely converted to monomeric form on immunoblot patterns. It appeared that some of the secreted factor XII Tenri formed several types of disulfide-linked complexes, including a factor XII-{alpha}1-microglobulin complex, through a newly generated Cys residue. The monomeric form of factor XII Tenri, like normal factor XII, was degraded into 2 major fragments with molecular weights of approximately 45 kDa and 30 kDa following mixing with activated partial-thromboplastin-time measuring reagent (cephalin and ellagic acid), whereas the factor XII Tenri that formed the complexes was not. This indicates that the factor XII Tenri present in disulfide-linked complexes with other proteins (and itself) is not converted to active forms, suggesting that attached proteins obstruct or delay the activation of factor XII via an inhibition of its binding to a negatively charged surface in vitro.

Keywords: factor XII deficiency, thromboembolism, activated partial thromboplastin time






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by the Association of Clinical Scientists.